Data detailing the platelet acetyl-lysine proteome

Joseph E. Aslan; Larry L. David; Owen J.T. McCarty

doi:10.1016/j.dib.2015.09.020

Data detailing the platelet acetyl-lysine proteome

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Abstract

Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification - mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation. Additionally, as platelets are anucleate and lack histone proteins, they offer a unique and valuable system to study the regulation of cytosolic proteins by lysine acetylation. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (Vizcaino et al., 2014 [2]) via with PRIDE partner repository with the dataset identifier PXD002332.

Original language	English (US)
Pages (from-to)	368-371
Number of pages	4
Journal	Data in Brief
Volume	5
DOIs	https://doi.org/10.1016/j.dib.2015.09.020
State	Published - Dec 1 2015

Funding

We thank P. Wilmarth (OHSU) for assistance with proteomics analyses. Proteomics studies were supported by a Research Core award from the OHSU School of Medicine , and NIH Grants P30EY010572, P30CA069533, and S10OD012246 . This work was supported by Grants from the National Institutes of Health ( R01HL101972 to O.J.T.M.), the American Heart Association ( 13POST13730003 to J.E.A. and 13EIA12630000 to O.J.T.M). The authors have no conflicts of interest to declare.

Funders	Funder number
OHSU School of Medicine
Author National Institutes of Health National Institutes of Health National Institutes of Health National Institutes of Health The Bev Hartig Huntington's Disease Foundation National Institutes of Health	R01HL101972
Author National Institutes of Health National Institutes of Health National Institutes of Health National Institutes of Health The Bev Hartig Huntington's Disease Foundation National Institutes of Health	P30CA069533, P30EY010572, S10OD012246
American Heart Association/American Stroke Association	13EIA12630000, 13POST13730003

Keywords

Acetylation
Hemostasis
Platelets
Proteomics

ASJC Scopus subject areas

General

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10.1016/j.dib.2015.09.020

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title = "Data detailing the platelet acetyl-lysine proteome",

abstract = "Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification - mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation. Additionally, as platelets are anucleate and lack histone proteins, they offer a unique and valuable system to study the regulation of cytosolic proteins by lysine acetylation. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (Vizcaino et al., 2014 [2]) via with PRIDE partner repository with the dataset identifier PXD002332.",

keywords = "Acetylation, Hemostasis, Platelets, Proteomics",

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year = "2015",

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doi = "10.1016/j.dib.2015.09.020",

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AU - Aslan, Joseph E.

AU - David, Larry L.

AU - McCarty, Owen J.T.

PY - 2015/12/1

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N2 - Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification - mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation. Additionally, as platelets are anucleate and lack histone proteins, they offer a unique and valuable system to study the regulation of cytosolic proteins by lysine acetylation. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (Vizcaino et al., 2014 [2]) via with PRIDE partner repository with the dataset identifier PXD002332.

AB - Here we detail proteomics data that describe the acetyl-lysine proteome of blood platelets (Aslan et al., 2015 [1]). An affinity purification - mass spectrometry (AP-MS) approach was used to identify proteins modified by Nε-lysine acetylation in quiescent, washed human platelets. The data provide insights into potential regulatory mechanisms of platelet function mediated by protein lysine acetylation. Additionally, as platelets are anucleate and lack histone proteins, they offer a unique and valuable system to study the regulation of cytosolic proteins by lysine acetylation. The mass spectrometry proteomics data have been deposited to the ProteomeXchange Consortium (Vizcaino et al., 2014 [2]) via with PRIDE partner repository with the dataset identifier PXD002332.

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KW - Hemostasis

KW - Platelets

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Data detailing the platelet acetyl-lysine proteome

Abstract

Funding

Keywords

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